Crystal Structure of High-Affinity von Willebrand Factor A1 domain with R1306Q and I1309V Mutations in Complex with High Affinity GPIb alpha. Determined by X-ray diffraction at 2.08 Å resolution. Released 8 Jan 2014.
Explore 4C2A in 3D Show helices and sheets RCSB PDB PDBe
4C2A contains 18 α-helices and 29 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1274 | 1 | 1 |
| β-strand | 1276-1283 | 8 | 2 |
| β-strand | 1285 | 1 | 3 |
| α-helix | 1290-1306 | 17 | |
| β-strand | 1314-1321 | 8 | 2 |
| β-strand | 1325-1329 | 5 | 2 |
| α-helix | 1337-1345 | 9 | |
| α-helix | 1347-1349 | 3 | |
| β-strand | 1352 | 1 | 3 |
| α-helix | 1357-1363 | 7 | |
| α-helix | 1364-1368 | 5 | |
| β-strand | 1378-1385 | 8 | 2 |
| α-helix | 1391-1393 | 3 | |
| α-helix | 1397-1406 | 10 | |
| β-strand | 1409-1416 | 8 | 2 |
| α-helix | 1422-1431 | 10 | |
| β-strand | 1438-1440 | 3 | 2 |
| α-helix | 1443-1445 | 3 | |
| α-helix | 1446-1460 | 15 | |
| α-helix | 1462 | 1 | |
| β-strand | 1463 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-9 | 5 | 4 |
| β-strand | 12-16 | 5 | 4 |
| α-helix | 25-26 | 2 | |
| β-strand | 35-37 | 3 | 4 |
| β-strand | 45-47 | 3 | 5 |
| α-helix | 48-51 | 4 | |
| β-strand | 59-61 | 3 | 4 |
| β-strand | 69-71 | 3 | 5 |
| β-strand | 81-83 | 3 | 4 |
| β-strand | 104-106 | 3 | 4 |
| β-strand | 128-130 | 3 | 4 |
| β-strand | 152-154 | 3 | 4 |
| β-strand | 176-178 | 3 | 4 |
| β-strand | 199-201 | 3 | 4 |
| β-strand | 207 | 1 | 6 |
| α-helix | 211-213 | 3 | |
| α-helix | 214-222 | 9 | |
| α-helix | 224-226 | 3 | |
| β-strand | 227 | 1 | 4 |
| β-strand | 228-233 | 6 | 2 |
| β-strand | 236-241 | 6 | 2 |
| α-helix | 243-245 | 3 | |
| β-strand | 247 | 1 | 7 |
| β-strand | 248 | 1 | 6 |
| β-strand | 255 | 1 | 7 |
| α-helix | 256-258 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Von willebrand factor | A | protein | 215 | HOMO SAPIENS | P04275 (AlphaFold model) |
| Platelet glycoprotein ib alpha chain | B | protein | 291 | HOMO SAPIENS | P07359 (AlphaFold model) |
>4C2A_1 VON WILLEBRAND FACTOR (chains A) MEPPLHDFYCSRLLDLVFLLDGSSRLSEAEFEVLKAFVVDMMEQLRVSQKWVRVAVVEYH DGSHAYIGLKDRKRPSELRRIASQVKYAGSQVASTSEVLKYTLFQIFSKIDRPEASRIAL LLMASQEPQRMSRNFVRYVQGLKKKKVIVIPVGIGPHANLKQIRLIEKQAPENKAFVLSS VDELEQQRDEIVSYLCDLAPEAPPPTLPPHHHHHH
>4C2A_2 PLATELET GLYCOPROTEIN IB ALPHA CHAIN (chains B) HPICEVSKVASHLEVNCDKRRLTALPPDLPKDTTILHLSENLLYTFSLATLMPYTRLTQL NLDRCELTKLQVDGTLPVLGTLDLSHNQLQSLPLLGQTLPALTVLDVSFNRLTSLPLGAL RGLGELQELYLKGNELKTLPPGLLTPTPKLEKLSLANNRLTELPAGLLNGLENLDTLLLQ ENSLYTIPKGFFGSHLLPFAFLHGNPWLCNCEILYFRRWLQDNAENVYVWKQVVDVKAVT SNVASVQCDNSDKFPVYKYPGKGCPTLGDEGDTDLYDYYPEEDTEGDKVRG
Water and common crystallization additives (ACT, PEG) are not listed.
Towards the Structural Basis of Regulation of Von Willebrand Factor Binding to Glycoprotein Ib. Blenner, M.A., Dong, X., Springer, T.A. J Biol Chem (2014) 289:5565. DOI 10.1074/JBC.M113.511220 · PubMed
Other PDB entries of the same protein (UniProt P04275 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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